Studying the detailed structural and functional characterization of different types of glycans is essential to understand the mechanism of various biological activities and the pathology of several diseases. CD BioGlyco has been trying to develop simple and effective enzymatic methods to release glycans from complex biological samples. We expect to be your research assistant in the field of glycobiology.
Glycosylation is an important way of post-translational modification of proteins, which has a variety of biological functions, such as immune recognition, signal transduction, cell adhesion, and tumorigenesis. Therefore, the development of effective methods to release glycans from the protein backbone is of great significance to the study of their structure and function.
In contrast to chemical methods of glycan release, enzymatic release can be carried out with minimum instructions in any laboratory. In the past two decades, more and more enzymes including endoglycosidases and glycosidases have been reported to release glycans from glycoproteins under mild conditions. The endoglycosidase endo-β-N-acetylglucosaminidase H (Endo H), peptide-N4-(acetyl-β-glucosaminyl) asparagine amidase F (PNGase F), and PNGase A are the most preferred endoglycosidases, N-glycans can be conveniently and non-selectively released from glycoproteins using these enzymes.
Enzymes are useful for the structural analysis of glycans and polysaccharides and for establishing structure-activity relationships in biological systems. To better characterize glycans on proteins, CD BioGlyco has developed an advanced glycan enzymatic release platform. We provide efficient and accurate release services of N-glycan, fucose, galactose, N-acetylgalactosamine (GalNAc), O-glycosylated protein, core-1 O-glycan, and sialic acid for our clients.
CD BioGlyco provides clients with efficient and accurate N-glycan release services on antibodies, fusion proteins, and other N-glycosylated proteins via PNGase F.
We efficiently release α1-2, α1-3, and α1-4 linked fucose present on N-glycosylated proteins, O-glycosylated proteins, or free oligosaccharides by fucosidase.
CD BioGlyco efficiently and accurately releases β1-3 and β1-4 linked galactose attached to N-glycans and O-glycans. Welcome to cooperate with us!
CD BioGlyco has integrated various technologies to develop an advanced glycan enzymatic release platform. We provide our clients with efficient and accurate GalNAc release services.
CD BioGlyco high-specifically hydrolyzes peptide bonds in proteins at the N-terminus of O-glycans at Ser or Thr via O-protease to release intact native core 1 O-glycosylated proteins.
At CD BioGlyco, we have developed an advanced glycan release platform to provide our clients with efficient and accurate release services of core 1 O-glycans from native glycoproteins.
CD BioGlyco focuses on teamwork and uses first-class experimental platforms to provide global biotechnology companies and scientific research institutions with efficient and high-quality services related to glycobiology. Our fast and effective solutions will greatly accelerate the progress of our clients' projects. Please contact us directly for more detailed information if you need scientific assistance.